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Carbonic anhydrase II (carbonate dehydratase) (hca II) (E.C.4.2.1.1) mutant with leu 198 replaced by arg (L198R)

Analyse Carbonic anhydrase II (carbonate dehydratase) (hca II) (E.C.4.2.1.1) mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1HEA
Type: protein
Length: 256 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carbonic anhydrase II
EC: 4.2.1.1
UniProt: P00918
Ligands: ZN, HG
Pockets: 1 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carbonic anhydrase II (EC 4.2.1.1)	protein	256	16% helix, 30% strand	P00918

Ligands and binding sites

ZN · Zinc ion · metal · chains A
HG · Mercury (II) ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	67	0.47	0.83	24	empty

Compared structures

1HEA · Carbonic anhydrase II (carbonate dehydratase) (hca II) (E.C.4.2.1.1) mutant with leu 198… · the same entry in another collection · chain A against A, TM-score 1.00
P00918 · AlphaFold monomer V2.0 prediction for carbonic anhydrase 2 (P00918) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P00918
Elsewhere: RCSB PDB 1HEA · PDBe 1HEA · UniProt P00918

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